Literature DB >> 7217674

A fluorescent assay for complement activation.

L H Caporale, S S Gaber, W Kell, O Götze.   

Abstract

We report here a rapid assay for the complement enzymes CVFBb, C4b2a and Cls. This assay involves the use of a peptide substrate that releases a fluorescent coumarin derivative (AMC) upon cleavage by the convertase. The substrate, BocLeuGlyArgAMC, was chosen because its sequence is similar to the carboxyl terminus of C3a, and identical to that of C5a. The Km of this substrate are about 125 microM for the C3/5 convertase CVFBb, 169 microM for C4b2a, and 140 microM for C1s.

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Year:  1981        PMID： 7217674

Source DB:  PubMed          Journal:  J Immunol        ISSN： 0022-1767            Impact factor:   5.422


  4 in total

1.  Effect of N-methylation on the modulation by synthetic peptides of the activity of the complement-factor-B-derived serine proteinase CVFBb.

Authors:  A Berkovich; M C O'Keefe; P Hensley; L Caporale
Journal:  Biochem J       Date:  1990-09-01       Impact factor: 3.857

2.  Proteases released in organ culture by acute dermal inflammatory lesions produced in vivo in rabbit skin by sulfur mustard: hydrolysis of synthetic peptide substrates for trypsin-like and chymotrypsin-like enzymes.

Authors:  K Higuchi; A Kajiki; M Nakamura; S Harada; P J Pula; A L Scott; A M Dannenberg
Journal:  Inflammation       Date:  1988-08       Impact factor: 4.092

3.  Complement activation by whole endotoxin is blocked by a monoclonal antibody to factor B.

Authors:  C W Clardy
Journal:  Infect Immun       Date:  1994-10       Impact factor: 3.441

4.  Detection of serine proteases in extracts of the domestic mite Blomia tropicalis.

Authors:  Federico Montealegre; Carmen Quiñones; Nanette Torres; Kirsteen Goth
Journal:  Exp Appl Acarol       Date:  2002       Impact factor: 2.380
  4 in total

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